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Details on Person Integrin alphaVbeta3 is sometimes referred to as the 'vitron...

Class:IdSummation:2426455
_displayNameIntegrin alphaVbeta3 is sometimes referred to as the 'vitron...
_timestamp2013-08-02 10:10:34
created[InstanceEdit:2426542] Jupe, S, 2012-08-03
literatureReference[LiteratureReference:215834] Alpha v beta 1 is a receptor for vitronectin and fibrinogen, and acts with alpha 5 beta 1 to mediate spreading on fibronectin
[LiteratureReference:2396075] A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin
[LiteratureReference:4085129] Distinct ligand-binding modes for integrin alpha(v)beta(3)-mediated adhesion to fibronectin versus vitronectin
[LiteratureReference:2396446] The alpha v beta 5 integrin receptor regulates receptor-mediated endocytosis of vitronectin
[LiteratureReference:2396163] Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors
[LiteratureReference:2466240] Human microvascular endothelial cells express integrin-related complexes that mediate adhesion to the extracellular matrix
[LiteratureReference:2466118] Detachment of cells from culture substrate by soluble fibronectin peptides
[LiteratureReference:2466181] Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
modified[InstanceEdit:2466194] Jupe, S, 2012-09-06
[InstanceEdit:2867920] Jupe, S, 2012-12-19
[InstanceEdit:4085125] Jupe, S, 2013-08-02
textIntegrin alphaVbeta3 is sometimes referred to as the 'vitronectin receptor'. Vitronectin interacts with integrins alphaVbeta1 (Marshall et al. 1995), alphaVbeta3 (Pytela et al. 1985, Boettiger et al. 2001), alphaVbeta5 (Panetti & McKeown-Longo 1993) and alpha2b beta3 (Pytela et al. 1986) through Arg-Gly-Asp (RGD) cell binding sequences.

Endothelial cells lining the microvascular wall form a semi-permeable barrier to the movement of blood components. The attachment of endothelial cells to the extracellular matrix (ECM) is largely mediated by transmembrane integrins which recognize short sequence motifs such as Arg-Gly-Asp (RGD) in many ECM proteins.

Integrin alpha5beta1 and alphaVbeta3 bind to the ECM proteins fibronectin and vitronectin respectively. Both are critical for the establishment and stabilization of endothelial monolayers (Cheng & Kramer 1989). Synthetic peptides that compete with ECM proteins for the integrins or antibodies directed against alpha5beta1 and alphaVbeta3 cause endothelial cell detachment (Hayman et al. 1985, Pierschbacher & Ruoslahti 1987).
(summation)[Reaction:2426471] VTN binds integrins alphaVbeta1, alphaVbeta3, alpha3beta5, alphaIIBbeta3 [Homo sapiens]
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